Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMF97306.1 | AMG00239.1 | AL538_05850 | AL538_21315 | Murein transglycosylase; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. | Flagellar hook-associated protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | 0.456 |
| AMF97306.1 | AMG01124.1 | AL538_05850 | AL538_26060 | Murein transglycosylase; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. | Chemotaxis protein CheC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.416 |
| AMF97306.1 | fliD | AL538_05850 | AL538_05150 | Murein transglycosylase; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. | Flagellar capping protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | 0.456 |
| AMF97306.1 | fliE | AL538_05850 | AL538_05120 | Murein transglycosylase; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. | Flagellar hook-basal body protein FliE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.441 |
| AMF97306.1 | fliE-2 | AL538_05850 | AL538_21380 | Murein transglycosylase; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. | Flagellar hook-basal body protein FliE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.441 |
| AMF97306.1 | glpD | AL538_05850 | AL538_05845 | Murein transglycosylase; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. | Glycerol-3-phosphate dehydrogenase; In Escherichia coli this homodimeric enzyme is expressed under aerobic conditions; anaerobic expression is repressed by the arcAB system; converts sn-glycerol-3-phosphate and ubiquinone-8 to dihydroxy acetone phosphate and ubiquinol-8; associates with the cytoplasmic membrane; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family. | 0.458 |
| AMG00239.1 | AMF97306.1 | AL538_21315 | AL538_05850 | Flagellar hook-associated protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Murein transglycosylase; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. | 0.456 |
| AMG00239.1 | AMG01124.1 | AL538_21315 | AL538_26060 | Flagellar hook-associated protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Chemotaxis protein CheC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.885 |
| AMG00239.1 | fliD | AL538_21315 | AL538_05150 | Flagellar hook-associated protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar capping protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | 0.924 |
| AMG00239.1 | fliE | AL538_21315 | AL538_05120 | Flagellar hook-associated protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar hook-basal body protein FliE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.897 |
| AMG00239.1 | fliE-2 | AL538_21315 | AL538_21380 | Flagellar hook-associated protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar hook-basal body protein FliE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.878 |
| AMG01124.1 | AMF97306.1 | AL538_26060 | AL538_05850 | Chemotaxis protein CheC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Murein transglycosylase; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. | 0.416 |
| AMG01124.1 | AMG00239.1 | AL538_26060 | AL538_21315 | Chemotaxis protein CheC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar hook-associated protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | 0.885 |
| AMG01124.1 | fliD | AL538_26060 | AL538_05150 | Chemotaxis protein CheC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar capping protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | 0.885 |
| AMG01124.1 | fliE | AL538_26060 | AL538_05120 | Chemotaxis protein CheC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar hook-basal body protein FliE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.875 |
| AMG01124.1 | fliE-2 | AL538_26060 | AL538_21380 | Chemotaxis protein CheC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar hook-basal body protein FliE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.875 |
| fliD | AMF97306.1 | AL538_05150 | AL538_05850 | Flagellar capping protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Murein transglycosylase; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. | 0.456 |
| fliD | AMG00239.1 | AL538_05150 | AL538_21315 | Flagellar capping protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar hook-associated protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | 0.924 |
| fliD | AMG01124.1 | AL538_05150 | AL538_26060 | Flagellar capping protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Chemotaxis protein CheC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.885 |
| fliD | fliE | AL538_05150 | AL538_05120 | Flagellar capping protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar hook-basal body protein FliE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.925 |
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